Enzyme

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EC Tree
     1. Oxidoreductases
        1.4 Acting on the CH-NH2 group of donors
            1.4.5 With a quinone or other compound as acceptor
ID:1.4.5.1
Description:D-amino acid dehydrogenase (quinone).
Alternative Name: DadA.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.4.5.1
BRENDA Enzyme Link: BRENDA 1.4.5.1
KEGG Enzyme Link: KEGG1.4.5.1
BioCyc Enzyme Link: BioCyc 1.4.5.1
ExPASy Enzyme Link: ExPASy1.4.5.1
EC2PDB Enzyme Link: EC2PDB 1.4.5.1
ExplorEnz Enzyme Link: ExplorEnz 1.4.5.1
PRIAM enzyme-specific profiles Link: PRIAM 1.4.5.1
IntEnz Enzyme Link: IntEnz 1.4.5.1
MEDLINE Enzyme Link: MEDLINE 1.4.5.1
MSA:

1.4.5.1;

Phylogenetic Tree:

1.4.5.1;

Uniprot:
M-CSA:
RHEA:45996 a D-amino acid + a quinone + H2O = a 2-oxocarboxylate + a quinol + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[O;H0;+0:5]=[C;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[C;H0;+0:9](=[O;H0;+0:10])-[CH;+0:11]=[CH;+0:12]-1.[OH2;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:13].[NH3;+0:4].[OH;+0:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[OH;+0:10]):[cH;+0:11]:[cH;+0:12]:1
Reaction
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References

TitleAuthorsDatePubMed ID
D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637.Tanigawa M, Shinohara T, Saito M, Nishimura K, Hasegawa Y, Wakabayashi S, Ishizuka M, Nagata Y2010 Jan19212808
Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B.Olsiewski PJ, Kaczorowski GJ, Walsh C1980 May 256102989